Kurjan J, Herskowitz I
Cell. 1982 Oct;30(3):933-43. doi: 10.1016/0092-8674(82)90298-7.
We have cloned and sequenced a gene (MF alpha) coding for alpha-factor, a tridecapeptide mating factor secreted by yeast alpha cells. A plasmid carrying the MF alpha gene was identified by screening for production of alpha-factor by mat alpha 2 mutants, which fail to secrete alpha-factor because of simultaneous synthesis and degradation of the factor. The cloned segment codes for four mature alpha-factor within a putative precursor of 165 amino acids. The putative precursor begins as a signal sequence for secretion. The next segment, of approximately 60 amino acids, contains three potential glycosylation sites. The carboxy-terminal half of the precursor contains four tandem copies of mature alpha-factor, each preceded by spacer peptides of six or eight amino acids (variations of Lys-Arg-Glu-Ala-Asp-Ala-Glu-Ala), which are hypothesized to contain proteolytic processing signals.
我们已经克隆并测序了一个编码α因子的基因（MFα），α因子是酵母α细胞分泌的一种十三肽交配因子。通过筛选matα2突变体产生α因子来鉴定携带MFα基因的质粒，matα2突变体由于该因子的同时合成和降解而无法分泌α因子。克隆片段在一个165个氨基酸的假定前体中编码四个成熟的α因子。假定的前体起始于一个分泌信号序列。接下来大约60个氨基酸的片段包含三个潜在的糖基化位点。前体的羧基末端一半包含四个成熟α因子的串联拷贝，每个拷贝之前都有六个或八个氨基酸的间隔肽（赖氨酸-精氨酸-谷氨酸-丙氨酸-天冬氨酸-丙氨酸-谷氨酸-丙氨酸的变体），据推测这些间隔肽包含蛋白水解加工信号。
